Yeast RNA polymerase I: A eukaryotic zinc metalloenzyme

Microwave excitation spectrometry and metal binding inhibition studies show that zinc is a catlytically essential component of the highly purified RNA polymerase I from yeast, the first eukaryotic RNA polymerase I available in quantities sufficient for such studies. It contains 2.4 g-atom of zinc based on a molecular weight of 6.5 × 10⁵ (8). Copper, iron, manganese and magnesium are absent, i.e., below the limits of detection, 10^?13 to 10^?14 g-atoms. A number of derivatives of 1,10-phenanthroline reversibly inhibit the polymerase catalyzed reaction, apparently by forming a ternary polymerase·Zn·OP complex while the nonchelating isomer, 1,7-phenanthroline, is ineffective.